Structure-based, targeted deglycosylation of HIV-1 gp120 and effects on neutralization sensitivity and antibody recognition

The human immunodeficiency virus (HIV-1) exterior envelope glycoprotein, gp120, mediates receptor binding and is the major target for neutralizing antibodies. Primary HIV-1 isolates are characteristically more resistant to broadly neutralizing antibodies, although the structural basis for this resis...

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Veröffentlicht in:	Virology (New York, N.Y.) N.Y.), 2003-09, Vol.313 (2), p.387-400
Hauptverfasser:	Koch, Markus, Pancera, Marie, Kwong, Peter D, Kolchinsky, Peter, Grundner, Christoph, Wang, Liping, Hendrickson, Wayne A, Sodroski, Joseph, Wyatt, Richard
Format:	Artikel
Sprache:	eng
Schlagworte:	Antibody binding Binding Sites CD4 Antigens - immunology Correlation Deglycosylation Exterior envelope glycoprotein Gene Deletion Glycosylation HIV Antibodies - immunology HIV Envelope Protein gp120 - chemistry HIV Envelope Protein gp120 - genetics HIV Envelope Protein gp120 - immunology HIV-1 HIV-1 - chemistry HIV-1 - immunology Humans Immunoglobulin Variable Region Models, Molecular Neutralization Neutralization Tests Polysaccharides - analysis Structure
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